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Volumn 18, Issue 5, 1998, Pages 3044-3058

Activation of Rho-dependent cell spreading and focal adhesion biogenesis by the v-Crk adaptor protein

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; NERVE GROWTH FACTOR; RHO FACTOR;

EID: 0031897657     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.18.5.3044     Document Type: Article
Times cited : (67)

References (79)
  • 2
    • 0029937918 scopus 로고    scopus 로고
    • Src, ras, and rac mediate the migratory response elicited by NGF and PMA in PC12 cells
    • Altun-Gultekin, Z. F., and J. A. Wagner. 1996. Src, ras, and rac mediate the migratory response elicited by NGF and PMA in PC12 cells. J. Neurosci. Res. 44:308-327.
    • (1996) J. Neurosci. Res. , vol.44 , pp. 308-327
    • Altun-Gultekin, Z.F.1    Wagner, J.A.2
  • 5
    • 0021879488 scopus 로고
    • Focal contacts of normal and RSV-transformed quail cells. Hypothesis of the transformation-induced deficient maturation of focal contacts
    • Bershadsky, A. D., I. S. Tint, A. A. Neyfakh, Jr., and J. M. Vasiliev. 1985. Focal contacts of normal and RSV-transformed quail cells. Hypothesis of the transformation-induced deficient maturation of focal contacts. Exp. Cell Res. 158:433-444.
    • (1985) Exp. Cell Res. , vol.158 , pp. 433-444
    • Bershadsky, A.D.1    Tint, I.S.2    Neyfakh Jr., A.A.3    Vasiliev, J.M.4
  • 6
    • 0030180321 scopus 로고    scopus 로고
    • SH2- And SH3-containing adaptor proteins: Redundant or independent mediators of intracellular signal transduction
    • Birge, R. B., B. S. Knudsen, D. Besser, and H. Hanafusa. 1996. SH2-and SH3-containing adaptor proteins: redundant or independent mediators of intracellular signal transduction. Gene Cell 1:595-613.
    • (1996) Gene Cell , vol.1 , pp. 595-613
    • Birge, R.B.1    Knudsen, B.S.2    Besser, D.3    Hanafusa, H.4
  • 7
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of rac/rho GTP-binding proteins
    • Bokoch, G. M., B. P. Bohl, and T.-H. Chuang. 1994. Guanine nucleotide exchange regulates membrane translocation of rac/rho GTP-binding proteins. J. Biol. Chem. 269:31674-31679.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.-H.3
  • 9
    • 0026445719 scopus 로고
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119:893-903.
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 11
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • Chong, L. D., A. Traynor-Kaplan, G. M. Bokoch, and M. A. Schwartz. 1994. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell 79:507-513.
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 12
    • 0029890229 scopus 로고    scopus 로고
    • The 70 kDa S6 kinase complexes with and is activated by the Rho family G proteins Cdc42 and Rac1
    • Chou, M. M., and J. Blenis. 1996. The 70 kDa S6 kinase complexes with and is activated by the Rho family G proteins Cdc42 and Rac1. Cell 85:573-583.
    • (1996) Cell , vol.85 , pp. 573-583
    • Chou, M.M.1    Blenis, J.2
  • 13
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M., and K. Burridge. 1996. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133:1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 14
    • 0031033292 scopus 로고    scopus 로고
    • Phosphotyrosine-dependent activation of rac-1 GDP/GTP exchange by the vav proto-oncogene product
    • Crespo, P., K. E. Schuebel, A. A. Ostrom, J. S. Gutkind, and X. R. Bustelo. 1997. Phosphotyrosine-dependent activation of rac-1 GDP/GTP exchange by the vav proto-oncogene product. Nature (London) 385:169-172.
    • (1997) Nature (London) , vol.385 , pp. 169-172
    • Crespo, P.1    Schuebel, K.E.2    Ostrom, A.A.3    Gutkind, J.S.4    Bustelo, X.R.5
  • 15
    • 0028170046 scopus 로고
    • Specific roles of the alpha V beta 1, alpha V beta 3, and alpha V beta 5 integrins in avian neural crest cell adhesion and migration on vitronectin
    • Delannet, M., F. Martin, B. Bossy, D. A. Cheresh, L. F. Reichardt, and J. L. Duband. 1994. Specific roles of the alpha V beta 1, alpha V beta 3, and alpha V beta 5 integrins in avian neural crest cell adhesion and migration on vitronectin. Development 120:2687-2702.
    • (1994) Development , vol.120 , pp. 2687-2702
    • Delannet, M.1    Martin, F.2    Bossy, B.3    Cheresh, D.A.4    Reichardt, L.F.5    Duband, J.L.6
  • 16
    • 0040106980 scopus 로고
    • The distribution of distinct integrins in focal contacts is determined by the substratum composition
    • Fath, K. R., C.-J. S. Edgell, and K. Burridge. 1989. The distribution of distinct integrins in focal contacts is determined by the substratum composition. J. Cell Sci. 92:67-75.
    • (1989) J. Cell Sci. , vol.92 , pp. 67-75
    • Fath, K.R.1    Edgell, C.-J.S.2    Burridge, K.3
  • 17
    • 0029163077 scopus 로고
    • Detection of SH3 binding proteins in total cell lysates with GST-SH3 fusion proteins
    • Feller, S. M., B. Knudsen, T. W. Wong, and H. Hanafusa. 1995. Detection of SH3 binding proteins in total cell lysates with GST-SH3 fusion proteins. Methods Enzymol. 255:369-378.
    • (1995) Methods Enzymol. , vol.255 , pp. 369-378
    • Feller, S.M.1    Knudsen, B.2    Wong, T.W.3    Hanafusa, H.4
  • 18
    • 0029892628 scopus 로고    scopus 로고
    • Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130, and paxillin
    • Flinn, H. M., and A. J. Ridley. 1996. Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130, and paxillin. J. Cell Sci. 109:1133-1141.
    • (1996) J. Cell Sci. , vol.109 , pp. 1133-1141
    • Flinn, H.M.1    Ridley, A.J.2
  • 19
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • Frisch, S. M., K. Vuori, E. Ruoslahti, and P. Chan-Hui. 1996. Control of adhesion-dependent cell survival by focal adhesion kinase. J. Cell Biol. 134: 793-799.
    • (1996) J. Cell Biol. , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.4
  • 20
    • 0030929149 scopus 로고    scopus 로고
    • Identification of a novel, putative Rho-specific GDP/GTP exchange factor and a RhoA-binding protein: Control of neuronal morphology
    • Gebbink, M. F. B. G., O. Kranenburg, M. Poland, F. P. G. van Horck, B. Houssa, and W. H. Moolenaar. 1997. Identification of a novel, putative Rho-specific GDP/GTP exchange factor and a RhoA-binding protein: control of neuronal morphology. J. Cell Biol. 137:1603-1613.
    • (1997) J. Cell Biol. , vol.137 , pp. 1603-1613
    • Gebbink, M.F.B.G.1    Kranenburg, O.2    Poland, M.3    Van Horck, F.P.G.4    Houssa, B.5    Moolenaar, W.H.6
  • 21
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidyl inositol 4,5-bisphosphate
    • Gilmore, A. P., and K. Burridge. 1996. Regulation of vinculin binding to talin and actin by phosphatidyl inositol 4,5-bisphosphate. Nature (London) 381: 531-535.
    • (1996) Nature (London) , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 22
    • 0031032348 scopus 로고    scopus 로고
    • V-Crk, an effector of the NGF signaling pathway, delays apoptotic cell death in neurotrophin-deprived PC12 cells
    • Glassman, R. H., B. L. Hempstead, L. Stainco-Coico, M. G. Steiner, H. Hanafusa, and R. B. Birge. 1997. v-Crk, an effector of the NGF signaling pathway, delays apoptotic cell death in neurotrophin-deprived PC12 cells. Cell Death Differ. 4:82-93.
    • (1997) Cell Death Differ. , vol.4 , pp. 82-93
    • Glassman, R.H.1    Hempstead, B.L.2    Stainco-Coico, L.3    Steiner, M.G.4    Hanafusa, H.5    Birge, R.B.6
  • 24
    • 0027207287 scopus 로고
    • Tyrosine kinase stimulated guanine nucleotide exchange activity of vav in T cell activation
    • Gulbins, E., K. M. Coggeshell, G. Baier, S. Katzav, P. Burn, and A. Altman. 1993. Tyrosine kinase stimulated guanine nucleotide exchange activity of vav in T cell activation. Science 260:822-825.
    • (1993) Science , vol.260 , pp. 822-825
    • Gulbins, E.1    Coggeshell, K.M.2    Baier, G.3    Katzav, S.4    Burn, P.5    Altman, A.6
  • 25
    • 0028170820 scopus 로고
    • Small GTP-binding proteins and the regulation of the actin cytoskeleton
    • Hall, A. 1994. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 10:31-54.
    • (1994) Annu. Rev. Cell Biol. , vol.10 , pp. 31-54
    • Hall, A.1
  • 26
    • 0031081425 scopus 로고    scopus 로고
    • Signaling through focal adhesion kinase
    • Hanks, S. K., and T. R. Polte. 1997. Signaling through focal adhesion kinase. Bioessays 19:137-145.
    • (1997) Bioessays , vol.19 , pp. 137-145
    • Hanks, S.K.1    Polte, T.R.2
  • 27
    • 0029117595 scopus 로고
    • Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets
    • Hartwig, J. H., G. M. Bokoch, C. L. Carpenter, P. A. Janmey, L. A. Taylor, A. Toker, and T. P. Stossel. 1995. Thrombin receptor ligation and activated rac uncap actin filament barbed ends through phosphoinositide synthesis in permeabilized human platelets. Cell 82:643-653.
    • (1995) Cell , vol.82 , pp. 643-653
    • Hartwig, J.H.1    Bokoch, G.M.2    Carpenter, C.L.3    Janmey, P.A.4    Taylor, L.A.5    Toker, A.6    Stossel, T.P.7
  • 28
    • 0028347526 scopus 로고
    • Expression of the v-Crk oncogene product in PC12 cells results in rapid differentiation by both nerve growth factor-dependent and epidermal growth factor-dependent pathways
    • Hempstead, B. L., R. B. Birge, J. E. Fajardo, R. Glassman, D. Mahadeo, R. Kraemer, and H. Hanafusa. 1994. Expression of the v-Crk oncogene product in PC12 cells results in rapid differentiation by both nerve growth factor-dependent and epidermal growth factor-dependent pathways. Mol. Cell Biol. 14:1964-1971.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1964-1971
    • Hempstead, B.L.1    Birge, R.B.2    Fajardo, J.E.3    Glassman, R.4    Mahadeo, D.5    Kraemer, R.6    Hanafusa, H.7
  • 29
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases
    • Hotchin, N. A., and A. Hall. 1995. The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases. J. Cell Biol. 131:1857-1865.
    • (1995) J. Cell Biol. , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 32
    • 0030615004 scopus 로고    scopus 로고
    • P160 rock, a rho-associated coiled-coil forming protein kinase, works downstream of rho and induces focal adhesions
    • Ishizaki, T., M. Naito, K. Fuzisawa, M. Maekawa, N. Watarabe, Y. Saito, and S. Narumiya. 1997. p160 rock, a rho-associated coiled-coil forming protein kinase, works downstream of rho and induces focal adhesions. FEBS Lett. 404:118-124.
    • (1997) FEBS Lett. , vol.404 , pp. 118-124
    • Ishizaki, T.1    Naito, M.2    Fuzisawa, K.3    Maekawa, M.4    Watarabe, N.5    Saito, Y.6    Narumiya, S.7
  • 33
    • 0026748742 scopus 로고
    • Thrombin receptor activation causes rapid cell rounding and neurite retraction independent of classic second messengers
    • Jalink, K., and W. H. Moolenaar. 1992. Thrombin receptor activation causes rapid cell rounding and neurite retraction independent of classic second messengers. J. Cell Biol. 118:411-419.
    • (1992) J. Cell Biol. , vol.118 , pp. 411-419
    • Jalink, K.1    Moolenaar, W.H.2
  • 34
    • 0028021308 scopus 로고
    • Inhibition of lysophosphatidate- and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein rho
    • Jalink, K., E. J. VanCorven, T. Hengeveld, N. Morii, S. Narumiya, and W. H. Moolenaar. 1994. Inhibition of lysophosphatidate-and thrombin-induced neurite retraction and neuronal cell rounding by ADP ribosylation of the small GTP-binding protein rho. J. Cell Biol. 126:801-810.
    • (1994) J. Cell Biol. , vol.126 , pp. 801-810
    • Jalink, K.1    VanCorven, E.J.2    Hengeveld, T.3    Morii, N.4    Narumiya, S.5    Moolenaar, W.H.6
  • 35
    • 0023157142 scopus 로고
    • Modulation of gelsolin function by phosphatidylinositol-4,5-bisphosphate
    • Janmey, P. A., and T. P. Stossel. 1987. Modulation of gelsolin function by phosphatidylinositol-4,5-bisphosphate. Nature (London) 325:362-365.
    • (1987) Nature (London) , vol.325 , pp. 362-365
    • Janmey, P.A.1    Stossel, T.P.2
  • 37
    • 0028606468 scopus 로고
    • Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first src homology 3 domain of Crk
    • Knudsen, B. S., S. M. Feller, and H. Hanafusa. 1994. Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first src homology 3 domain of Crk. J. Biol. Chem. 269: 32781-32787.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32781-32787
    • Knudsen, B.S.1    Feller, S.M.2    Hanafusa, H.3
  • 38
    • 0031027205 scopus 로고    scopus 로고
    • Rho family GTPases and neuronal growth cone remodelling: Relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid
    • Kozma, R., S. Sarner, S. Ahmed, and L. Lim. 1997. Rho family GTPases and neuronal growth cone remodelling: relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid. Mol. Cell. Biol. 17:1201-1211.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1201-1211
    • Kozma, R.1    Sarner, S.2    Ahmed, S.3    Lim, L.4
  • 39
    • 0027496730 scopus 로고
    • ADP-ribosylation of Rho p21 inhibits lysophosphatidic acid-induced protein tyrosine phosphorylation and phosphatidylinositol 3-kinase activation in Swiss 3T3 cells
    • Kumagai, N., N. Morii, K. Fujisawa, Y. Nemoto, and S. Narumiya. 1993. ADP-ribosylation of Rho p21 inhibits lysophosphatidic acid-induced protein tyrosine phosphorylation and phosphatidylinositol 3-kinase activation in Swiss 3T3 cells. J. Biol. Chem. 268:24535-24538.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24535-24538
    • Kumagai, N.1    Morii, N.2    Fujisawa, K.3    Nemoto, Y.4    Narumiya, S.5
  • 41
    • 0031058930 scopus 로고    scopus 로고
    • Pheromone signalling and polarized morphogenesis in yeast
    • Leberer, E., D. Y. Thomas, and M. Whiteway. 1997. Pheromone signalling and polarized morphogenesis in yeast. Curr. Opin. Genet. Dev. 7:59-66.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 59-66
    • Leberer, E.1    Thomas, D.Y.2    Whiteway, M.3
  • 42
    • 0029789678 scopus 로고    scopus 로고
    • The p 160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., X.-Q. Chen, E. Manser, and L. Lim. 1996. The p 160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16:5313-5327.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.-Q.2    Manser, E.3    Lim, L.4
  • 43
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the ras-related rhoA GTPase which translocates the kinase to peripheral membranes
    • Leung, T., E. Manser, L. Tan, and L. Lim. 1995. A novel serine/threonine kinase binding the ras-related rhoA GTPase which translocates the kinase to peripheral membranes. J. Biol. Chem. 270:29051-29054.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 44
    • 0030026182 scopus 로고    scopus 로고
    • Differential effects of the rac GTPase on Purkinje cell axons and dendritic trunks and spines
    • Luo, L., T. K. Hensch, L. Ackerman, S. Barbel, L. Y. Jan, and Y. N. Jan. 1996. Differential effects of the rac GTPase on Purkinje cell axons and dendritic trunks and spines. Nature (London) 379:837-840.
    • (1996) Nature (London) , vol.379 , pp. 837-840
    • Luo, L.1    Hensch, T.K.2    Ackerman, L.3    Barbel, S.4    Jan, L.Y.5    Jan, Y.N.6
  • 45
    • 0031065475 scopus 로고    scopus 로고
    • Rho family small GTP-binding proteins in growth cone signalling
    • Luo, L., L. Y. Jan, and Y.-N. Jan. 1997. Rho family small GTP-binding proteins in growth cone signalling. Curr. Opin. Neurobiol. 7:81-86.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 81-86
    • Luo, L.1    Jan, L.Y.2    Jan, Y.-N.3
  • 46
    • 0028086441 scopus 로고
    • Distinct morphogenetic functions of similar small GTPases: Drosophilia Drac1 is involved in axonal outgrowth and myoblast fusion
    • Luo, L., Y. J. Liao, J. Y. Jan, and Y. N. Jan. 1994. Distinct morphogenetic functions of similar small GTPases: Drosophilia Drac1 is involved in axonal outgrowth and myoblast fusion. Genes Dev. 8:1787-1802.
    • (1994) Genes Dev. , vol.8 , pp. 1787-1802
    • Luo, L.1    Liao, Y.J.2    Jan, J.Y.3    Jan, Y.N.4
  • 47
    • 0028829750 scopus 로고
    • The Rho's progress: A potential role during neuritogenesis for the Rho family of GTPases
    • Mackay, D. J. G., C. D. Nobes, and A. Hall. 1995. The Rho's progress: a potential role during neuritogenesis for the Rho family of GTPases. Trends Neurosci. 18:496-501.
    • (1995) Trends Neurosci. , vol.18 , pp. 496-501
    • Mackay, D.J.G.1    Nobes, C.D.2    Hall, A.3
  • 49
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser, E., T. Leung, H. Salihuddin, Z. Zhao, and L. Lim. 1994. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature (London) 367:40-46.
    • (1994) Nature (London) , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.4    Lim, L.5
  • 51
    • 0025352651 scopus 로고
    • Mutagenic analysis of the v-crk oncogene: Requirement for SH2 and SH3 domains and correlation between in-creased cellular phosphotyrosine and transformation
    • Mayer, B. J., and H. Hanafusa. 1990. Mutagenic analysis of the v-crk oncogene: requirement for SH2 and SH3 domains and correlation between in-creased cellular phosphotyrosine and transformation. J. Virol. 64:3581-3589.
    • (1990) J. Virol. , vol.64 , pp. 3581-3589
    • Mayer, B.J.1    Hanafusa, H.2
  • 55
  • 56
    • 0028961293 scopus 로고
    • Rho, rac and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and A. Hall. 1995. Rho, rac and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 57
    • 0028837170 scopus 로고
    • Activation of the small GTP-binding proteins rho and rac by growth factor receptors
    • Nobes, C. D., P. Hawkins, L. Stephens, and A. Hall. 1995. Activation of the small GTP-binding proteins rho and rac by growth factor receptors. J. Cell Sci. 108:225-233.
    • (1995) J. Cell Sci. , vol.108 , pp. 225-233
    • Nobes, C.D.1    Hawkins, P.2    Stephens, L.3    Hall, A.4
  • 58
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper, G. E., H. P. McNamee, L. E. Dike, K. Bojanowski, and D. E. Ingber. 1995. Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol. Biol. Cell 6:1349-1365.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 59
    • 0029889591 scopus 로고    scopus 로고
    • Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain
    • Reid, T., T. Furuyashiki, T. Ishizaki, G. Watanabe, N. Watanabe, K. Fujisawa, N. Morii, P. Madaule, and S. Narumiya. 1996. Rhotekin, a new putative target for Rho bearing homology to a serine/threonine kinase, PKN, and rhophilin in the rho-binding domain. J. Biol. Chem. 271:13556-13560.
    • (1996) J. Biol. Chem. , vol.271 , pp. 13556-13560
    • Reid, T.1    Furuyashiki, T.2    Ishizaki, T.3    Watanabe, G.4    Watanabe, N.5    Fujisawa, K.6    Morii, N.7    Madaule, P.8    Narumiya, S.9
  • 60
    • 0030001638 scopus 로고    scopus 로고
    • Physical association of the small GTPase rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells
    • Ren, X.-D., G. M. Bokoch, A. Traynor-Kaplan, G. H. Jenkins, R. A. Anderson, and M. A. Schwartz. 1996. Physical association of the small GTPase rho with a 68-kDa phosphatidylinositol 4-phosphate 5-kinase in Swiss 3T3 cells. Mol. Biol. Cell 7:435-442.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 435-442
    • Ren, X.-D.1    Bokoch, G.M.2    Traynor-Kaplan, A.3    Jenkins, G.H.4    Anderson, R.A.5    Schwartz, M.A.6
  • 61
    • 0028321785 scopus 로고
    • Signal transduction pathways regulating rho-mediated stress fibre formation: Requirement for a tyrosine kinase
    • Ridley, A. J., and A. Hall. 1994. Signal transduction pathways regulating rho-mediated stress fibre formation: requirement for a tyrosine kinase. EMBO J. 13:2600-2610.
    • (1994) EMBO J. , vol.13 , pp. 2600-2610
    • Ridley, A.J.1    Hall, A.2
  • 62
    • 0026778133 scopus 로고
    • The small GTP binding protein rho regulates the assembly of focal adhesions and stress fibers in response to growth factors
    • Ridley, A. J., and A. Hall. 1992. The small GTP binding protein rho regulates the assembly of focal adhesions and stress fibers in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 65
    • 0028944227 scopus 로고
    • Guanosine 5′-3′-O-(thio)triphosphate stimulates tyrosine phosphorylation of p125FAK and paxillin in permeabilized Swiss 3T3 cells
    • Seckl, M. J., N. Morii, S. Narumiya, and E. Rozengurt. 1995. Guanosine 5′-3′-O-(thio)triphosphate stimulates tyrosine phosphorylation of p125FAK and paxillin in permeabilized Swiss 3T3 cells. J. Biol. Chem. 270:6984-6990.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6984-6990
    • Seckl, M.J.1    Morii, N.2    Narumiya, S.3    Rozengurt, E.4
  • 66
    • 0026519282 scopus 로고
    • Thrombin causes neurite retraction in neural cells through activation of cell surface receptors
    • Suidan, H. S., S. R. Stone, B. A. Hemmings, and D. Monard. 1992. Thrombin causes neurite retraction in neural cells through activation of cell surface receptors. Neuron 8:363-375.
    • (1992) Neuron , vol.8 , pp. 363-375
    • Suidan, H.S.1    Stone, S.R.2    Hemmings, B.A.3    Monard, D.4
  • 69
    • 0031004266 scopus 로고    scopus 로고
    • Downstream of Crk adaptor signaling pathway: Activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G
    • Tanaka, S., T. Ouchi, and H. Hanafusa. 1997. Downstream of Crk adaptor signaling pathway: activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G. Proc. Natl. Acad. Sci. USA 94:2356-2361.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2356-2361
    • Tanaka, S.1    Ouchi, T.2    Hanafusa, H.3
  • 70
    • 0029152154 scopus 로고
    • V-crk modulation of growth factor-induced PC12 cell differentiation involves the src homology 2 domain of v-crk and sustained activation of the Ras/mitogen-activated protein kinase pathway
    • Teng, K. K., H. Lander, J. E. Fajardo, H. Hanafusa, B. L. Hempstead, and R. B. Birge. 1995. v-crk modulation of growth factor-induced PC12 cell differentiation involves the src homology 2 domain of v-crk and sustained activation of the Ras/mitogen-activated protein kinase pathway. J. Biol. Chem. 270:20677-20685.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20677-20685
    • Teng, K.K.1    Lander, H.2    Fajardo, J.E.3    Hanafusa, H.4    Hempstead, B.L.5    Birge, R.B.6
  • 72
    • 0026795116 scopus 로고
    • Lysophosphatidates bound to serum albumin activate membrane currents in Xenopus oocytes and neurite retraction in PC12 pheochromocytoma cells
    • Tigyi, G., and R. Miledi. 1992. Lysophosphatidates bound to serum albumin activate membrane currents in Xenopus oocytes and neurite retraction in PC12 pheochromocytoma cells. J. Biol. Chem. 267:21360-21367.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21360-21367
    • Tigyi, G.1    Miledi, R.2
  • 74
    • 0030894714 scopus 로고    scopus 로고
    • The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization
    • Vincent, S., and J. Settleman. 1997. The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization. Mol. Cell. Biol. 17:2247-2256.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2247-2256
    • Vincent, S.1    Settleman, J.2
  • 77
    • 0027370725 scopus 로고
    • Bombesin, vasopressin, and endothelin rapidly stimulate tyrosine phopshorylation of the focal adhesion-associated protein paxillin in Swiss 3T3 cells
    • Zachary, I., J. Sinnett-Smith, C. E. Turner, and E. Rozengurt. 1993. Bombesin, vasopressin, and endothelin rapidly stimulate tyrosine phopshorylation of the focal adhesion-associated protein paxillin in Swiss 3T3 cells. J. Biol. Chem. 268:22060-22065.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22060-22065
    • Zachary, I.1    Sinnett-Smith, J.2    Turner, C.E.3    Rozengurt, E.4
  • 78
    • 0027471434 scopus 로고
    • Expression of integrin α1 β1 is regulated by nerve growth factor and dexamethasone in PC12 cells. Functional consequences for adhesion and neurite outhgrowth
    • Zhang, Z., G. Tarone, and D. C. Turner. 1993. Expression of integrin α1 β1 is regulated by nerve growth factor and dexamethasone in PC12 cells. Functional consequences for adhesion and neurite outhgrowth. J. Biol. Chem. 268:5557-5565.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5557-5565
    • Zhang, Z.1    Tarone, G.2    Turner, D.C.3
  • 79
    • 0029783037 scopus 로고    scopus 로고
    • The pleckstrin homology domain mediates transformation by oncogenic dbl through specific intracellular targeting
    • Zheng, Y., D. Zangrilli, R. A. Cerione, and A. Eva. 1996. The pleckstrin homology domain mediates transformation by oncogenic dbl through specific intracellular targeting. J. Biol. Chem. 271:19017-19020.
    • (1996) J. Biol. Chem. , vol.271 , pp. 19017-19020
    • Zheng, Y.1    Zangrilli, D.2    Cerione, R.A.3    Eva, A.4


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